Medium-chain fatty-acid--CoA ligase
Details
- Name
- Medium-chain fatty-acid--CoA ligase
- Synonyms
- 6.2.1.-
- ACS
- Acyl-CoA synthetase
- Fatty acyl-CoA synthetase FadK
- ydiD
- Gene Name
- fadK
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0052024|Medium-chain fatty-acid--CoA ligase MHPTGPHLGPDVLFRESNMKVTLTFNEQRRAAYRQQGLWGDASLADYWQQTARAMPDKIA VVDNHGASYTYSALDHAASCLANWMLAKGIESGDRIAFQLPGWCEFTVIYLACLKIGAVS VPLLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDLILPLQNQLPQLQQIVGVDKLAP ATSSLSLSQIIADNTSLTTAITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCA RLNLTWQDVFMMPAPLGHATGFLHGVTAPFLIGARSVLLDIFTPDACLALLEQQRCTCML GATPFVYDLLNVLEKQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGSTESSPH AVVNLDDPLSRFMHTDGYAAAGVEIKVVDDARKTLPPGCEGEEASRGPNVFMGYFDEPEL TARALDEEGWYYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDA CVVAMSDERLGERSCAYVVLKAPHHSLSLEEVVAFFSRKRVAKYKYPEHIVVIEKLPRTT SGKIQKFLLRKDIMRRLTQDVCEEIE
- Number of residues
- 566
- Molecular Weight
- 62758.725
- Theoretical pI
- Not Available
- GO Classification
- FunctionsATP binding / medium-chain fatty acid-CoA ligase activityProcessesfatty acid beta-oxidationComponentsplasma membrane
- General Function
- Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids (PubMed:15213221, PubMed:19477415). Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor (PubMed:12535077). Can functionally replace FadD under anaerobic conditions (PubMed:12535077).
- Specific Function
- Atp binding
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cell membrane
- Gene sequence
>lcl|BSEQ0052025|Medium-chain fatty-acid--CoA ligase (fadK) ATGCATCCCACAGGCCCGCATCTCGGGCCTGATGTTCTGTTTCGAGAGTCCAACATGAAA GTGACATTAACGTTTAACGAACAACGTCGTGCGGCGTATCGTCAGCAAGGGTTATGGGGC GATGCTTCGCTGGCCGATTACTGGCAGCAGACCGCTCGTGCGATGCCAGACAAAATTGCC GTGGTCGATAATCATGGTGCATCGTACACCTATAGCGCGCTCGATCACGCCGCGAGCTGT CTGGCAAACTGGATGTTAGCGAAGGGTATTGAATCAGGCGATCGCATCGCATTTCAACTG CCTGGCTGGTGTGAATTTACCGTTATCTATCTTGCCTGCCTGAAAATCGGTGCAGTTTCC GTGCCGCTGTTGCCTTCCTGGCGGGAAGCAGAACTGGTGTGGGTGCTCAATAAGTGTCAG GCAAAAATGTTCTTTGCACCGACGTTGTTTAAACAAACGCGTCCGGTAGATTTAATCCTG CCGCTGCAAAATCAGCTTCCACAACTACAACAAATTGTCGGCGTGGACAAACTGGCTCCC GCCACCTCTTCCCTCTCATTAAGTCAGATTATCGCCGACAATACCTCACTGACCACGGCG ATAACGACCCACGGCGATGAATTAGCTGCGGTGCTGTTTACCTCCGGAACCGAGGGTCTG CCAAAGGGCGTGATGCTAACGCATAACAATATTCTCGCCAGTGAGCGGGCTTATTGCGCG CGACTGAATCTGACCTGGCAGGATGTCTTTATGATGCCTGCGCCACTTGGTCACGCAACG GGCTTTCTGCATGGCGTAACGGCACCATTCTTAATTGGCGCTCGCAGCGTGTTGTTAGAT ATTTTCACTCCTGATGCGTGTCTCGCGCTGCTTGAGCAGCAGCGTTGCACCTGTATGCTC GGCGCAACGCCGTTTGTCTATGATCTTTTGAATGTACTAGAGAAACAACCCGCGGACCTT TCAGCGCTGCGTTTCTTTCTTTGCGGCGGAACCACAATCCCCAAAAAAGTGGCGCGTGAA TGCCAGCAGCGCGGCATTAAATTATTAAGTGTTTATGGTTCCACAGAAAGTTCGCCGCAT GCGGTGGTGAATCTCGATGATCCTTTGTCGCGCTTTATGCACACCGATGGTTACGCTGCC GCAGGTGTAGAGATTAAAGTGGTCGATGACGCACGCAAGACCTTACCGCCAGGTTGCGAA GGTGAAGAAGCCTCGCGTGGCCCCAATGTGTTTATGGGGTATTTTGATGAACCTGAATTA ACCGCCCGTGCCCTGGATGAAGAAGGCTGGTATTACAGCGGCGATCTCTGCCGTATGGAT GAGGCTGGCTATATAAAAATTACCGGACGCAAAAAAGATATTATTGTCCGCGGCGGCGAA AATATTAGCAGCCGTGAAGTGGAAGATATTTTATTGCAGCATCCTAAAATTCACGATGCC TGTGTGGTTGCAATGTCCGATGAACGTTTAGGTGAACGATCATGCGCTTATGTCGTGCTG AAAGCGCCGCATCATTCATTATCGCTGGAAGAGGTAGTGGCTTTTTTTAGCCGTAAACGG GTCGCAAAATATAAATATCCTGAACATATCGTGGTAATCGAAAAACTACCGCGAACTACC TCAGGTAAAATACAAAAGTTTTTGTTAAGAAAAGATATTATGCGGCGTTTAACGCAGGAT GTCTGTGAAGAGATTGAATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P38135 UniProtKB Entry Name FADK_ECOLI - General References
- Aiba H, Baba T, Hayashi K, Inada T, Isono K, Itoh T, Kasai H, Kashimoto K, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Horiuchi T, et al.: A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):363-77. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Borodovsky M, Rudd KE, Koonin EV: Intrinsic and extrinsic approaches for detecting genes in a bacterial genome. Nucleic Acids Res. 1994 Nov 11;22(22):4756-67. [Article]
- Campbell JW, Morgan-Kiss RM, Cronan JE Jr: A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway. Mol Microbiol. 2003 Feb;47(3):793-805. [Article]
- Morgan-Kiss RM, Cronan JE: The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase. J Biol Chem. 2004 Sep 3;279(36):37324-33. doi: 10.1074/jbc.M405233200. Epub 2004 Jun 22. [Article]
- Leger M, Gavalda S, Guillet V, van der Rest B, Slama N, Montrozier H, Mourey L, Quemard A, Daffe M, Marrakchi H: The dual function of the Mycobacterium tuberculosis FadD32 required for mycolic acid biosynthesis. Chem Biol. 2009 May 29;16(5):510-9. doi: 10.1016/j.chembiol.2009.03.012. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details